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  Evidence for tautomerisation of glutamine in BLUF blue light receptors by vibrational spectroscopy and computational chemistry

Domratcheva, T., Hartmann, E., Schlichting, I., & Kottke, T. (2016). Evidence for tautomerisation of glutamine in BLUF blue light receptors by vibrational spectroscopy and computational chemistry. Scientific Reports, 6: 22669, pp. 1-14. doi:10.1038/srep22669.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-1B9C-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-29BA-A
Genre: Journal Article

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Domratcheva, Tatiana1, Author              
Hartmann, Elisabeth1, Author              
Schlichting, Ilme1, Author              
Kottke, Tilman, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: BLUF (blue light sensor using flavin) domains regulate the activity of various enzymatic effector domains in bacteria and euglenids. BLUF features a unique photoactivation through restructuring of the hydrogen-bonding network as opposed to a redox reaction or an isomerization of the chromophore. A conserved glutamine residue close to the flavin chromophore plays a central role in the light response, but the underlying modification is still unclear. We labelled this glutamine with 15N in two representative BLUF domains and performed time-resolved infrared double difference spectroscopy. The assignment of the signals was conducted by extensive quantum chemical calculations on large models with 187 atoms reproducing the UV-vis and infrared signatures of BLUF photoactivation. In the dark state, the comparatively low frequency of 1,667 cm−1 is assigned to the glutamine C=O accepting a hydrogen bond from tyrosine. In the light state, the signature of a tautomerised glutamine was extracted with the C=N stretch at ~1,691 cm−1 exhibiting the characteristic strong downshift by 15N labelling. Moreover, an indirect isotope effect on the flavin C4=O stretch was found. We conclude that photoactivation of the BLUF receptor does not only involve a rearrangement of hydrogen bonds but includes a change in covalent bonds of the protein.

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Language(s): eng - English
 Dates: 2015-12-042016-02-162016-03-07
 Publication Status: Published online
 Pages: 14
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 Table of Contents: -
 Rev. Method: Peer
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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 6 Sequence Number: 22669 Start / End Page: 1 - 14 Identifier: Other: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322